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Journal of Bacteriology, September 1999, p. 5557-5562, Vol. 181, No. 18
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Low-Temperature-Induced DnaA Protein Synthesis Does Not Change Initiation Mass in Escherichia coli K-12

T. Atlung1,* and F. G. Hansen2

Department of Life Sciences and Chemistry, Roskilde University, DK-4000 Roskilde,1 and Department of Microbiology, The Technical University of Denmark, DK-2800 Lyngby,2 Denmark

Received 26 March 1999/Accepted 2 July 1999

Expression of the dnaA gene continues in the lag phase following a temperature downshift, indicating that DnaA is a cold shock protein. Steady-state DnaA protein concentration increases at low temperatures, being twofold higher at 14°C than at 37°C. DnaA protein was found to be stable at both low and high temperatures. Despite the higher DnaA concentration at low temperatures, the mass per origin, which is proportional to the initiation mass, was the same at all temperatures. Cell size and cellular DNA content decreased moderately below 30°C due to a decrease in the time from termination to division relative to generation time at the lower temperatures. Analysis of dnaA gene expression and initiation of chromosome replication in temperature shifts suggests that a fraction of newly synthesized DnaA protein at low temperatures is irreversibly inactive for initiation and for autorepression or that all DnaA protein synthesized at low temperatures has an irreversible low-activity conformation.


* Corresponding author. Mailing address: Department of Life Sciences and Chemistry, Roskilde University, DK-4000 Roskilde, Denmark. Phone: (45) 46 74 24 02. Fax: (45) 46 74 30 11. E-mail: atlung{at}ruc.dk.


Journal of Bacteriology, September 1999, p. 5557-5562, Vol. 181, No. 18
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.



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